Related Experiment Video
Updated: Oct 21, 2025

Intracellular Refolding Assay
Published on: January 24, 2012
The interaction of heat shock proteins with cellular membranes: a historical perspective
Antonio De Maio1,2,3, Lawrence Hightower4
1Department of Surgery, Division of Trauma, Critical Care, Burns, and Acute Care Surgery, School of Medicine, University of California San Diego, La Jolla, CA, 92093, USA. ademaio@health.ucsd.edu.
Abstract:
The interaction of heat shock proteins (HSP) with cellular membranes has been an enigmatic process, initially observed by morphological studies, inferred during the purification of HSP70s, and confirmed after the detection of these proteins on the surface of cancer cells and their insertion into artificial lipid bilayers. Today, the association of several HSP with lipid membranes is well established. However, the mechanisms for membrane insertion have been elusive. There is conclusive evidence indicating that HSP70s have a great selectivity for negatively charged phospholipids, whereas other HSP have a broader spectrum of lipid specificity. HSP70 also oligomerizes upon membrane insertion, forming ion conductance channels. The functional role of HSP70 lipid interactions appears related to membrane stabilization that may play a role during cell membrane biogenesis. They could also play a role as membrane chaperones as well as during endocytosis, microautophagy, and signal transduction. Moreover, HSP membrane association is a key component in the extracellular export of these proteins. The presence of HSP70 on the surface of cancer cells and its interaction with lysosome membranes have been envisioned as potential therapeutic targets. Thus, the biology and function of HSP membrane association are reaching a new level of excitement. This review is an attempt to preserve the recollection of the pioneering contributions of many investigators that have participated in this endeavor.
Related Concept Videos
Molecular Chaperones and Protein Folding
The...
Diversity of Archaea IV
Responses to Heat and Cold Stress
Diversity of Archaea III
Bacterial Protein Maturation
Other Stress Responses in Bacteria

